Literature summary for 3.4.21.41 extracted from

Venkatraman Girija, U.; Gingras, A.R.; Marshall, J.E.; Panchal, R.; Sheikh, M.A.; Gal, P.; Schwaeble, W.J.; Mitchell, D.A.; Moody, P.C.; Wallis, R.
Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation (2013), Proc. Natl. Acad. Sci. USA, 110, 13916-13920.

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of full-length C1r protease and the CUB1-EGF-CUB2 fragment with low yield	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
zymogen C1s + H2O	Homo sapiens	-	active protease C1s + ?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00736	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme recognizes the a short collagen-like peptide containing the sequence Hyp-Gly-Lys-Leu-Gly-Pro	Homo sapiens	?	-	?
zymogen C1s + H2O	-	Homo sapiens	active protease C1s + ?	-	?

Synonyms

Synonyms	Comment	Organism
proteases C1r	-	Homo sapiens

General Information

General Information	Comment	Organism
evolution	binding residues are conserved in the CUB1 domains of C1r, MASP-1/-3, and MASP-2, indicating that the interaction mechanism is conserved in initiating complexes of the lectin and classical pathways	Homo sapiens
additional information	the large multicomponent assembly C1 complex is composed of a recognition subcomponent, C1q (460 kDa), and two serine protease subcomponents, C1r (90 kDa) and C1s (80 kDa) in a 1:2:2 ratio, with an overall molecular mass of about790 kDa. C1r is a modular protease with two N-terminal complement C1r/C1s, Uegf and bone morphogenetic protein-1(CUB) domains, separated by an epidermal growth factor (EGF)-ike domain, followed by two complement control modules (CCP) and a C-terminal serine protease (SP) domain	Homo sapiens
physiological function	the large multicomponent assembly C1 complex, binds to immune complexes, protein modulators (e.g., C-reactive protein), and polyanionic structures on pathogens to initiate complement activation. Binding to pathogens induces a conformational change that drives activation of the zymogen proteases in stepwise fashion: C1r first autoactivates, then activates C1s. C1s subsequently cleaves substrates C4 and C4b-bound C2, to form the C3 convertase (C4b2a), the downstream component of the reaction cascade	Homo sapiens

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Release 2023.1 (January 2023)